Previous GeneCards Identifiers for CDC25A Gene

Summaries for CDC25A Gene

Entrez Gene Summary for CDC25A Gene

CDC25A is a member of the CDC25 family of phosphatases. CDC25A is required for progression from G1 to the S phase of the cell cycle. It activates the cyclin-dependent kinase CDC2 by removing two phosphate groups. CDC25A is specifically degraded in response to DNA damage, which prevents cells with chromosomal abnormalities from progressing through cell division. CDC25A is an oncogene, although its exact role in oncogenesis has not been demonstrated. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]

GeneCards Summary for CDC25A Gene

CDC25A (Cell Division Cycle 25A) is a Protein Coding gene.
Among its related pathways are ERK Signaling and Cell Cycle, Mitotic.
GO annotations related to this gene include protein kinase binding and protein tyrosine phosphatase activity.
An important paralog of this gene is CDC25C.

UniProtKB/Swiss-Prot for CDC25A Gene

Tyrosine protein phosphatase which functions as a dosage-dependent inducer of mitotic progression. Directly dephosphorylates CDK1 and stimulates its kinase activity. Also dephosphorylates CDK2 in complex with cyclin E, in vitro

Tocris Summary for CDC25A Gene

Cdc25 is a dual specificity phosphatase with three isoforms in mammalian cells - cdc25A, B and C. Cdc25 activates cdk complexes that control progression through the cell cycle. Cdc25 is also involved in the DNA damage checkpoints. Regulation of cdc25 occurs through a variety of mechanisms including phosphorylation, interaction with 14.3.3 proteins, subcellular localization and protein degradation. Cdc25B is phosphorylated and activated by aurora kinase A at the start of mitosis, and as mitosis progresses is then further phosphorylated in an auto-amplification loop, along with cdc25C, by the CDK1/cyclin B complex. Cdc25C is also phosphorylated during mitosis by PLK1, leading to greater activity of the CDK1/cyclin B complex. Similarly, Cdc25A acts during the G1/S phase of the cell cycle in concert with the CDK2/cyclin E complex. Both cdc25A and cdc25B can be activated by the DNA damage checkpoint kinase, Chk1 and thereby inhibit mitosis.

Proteins for CDC25A Gene

Protein details for CDC25A Gene (UniProtKB/Swiss-Prot)

Protein attributes for CDC25A Gene

Size:

524 amino acids

Molecular mass:

59087 Da

Quaternary structure:

Interacts with CCNB1/cyclin B1. Interacts with YWHAE/14-3-3 epsilon when phosphorylated. Interacts with CUL1 specifically when CUL1 is neddylated and active. Interacts with BTRC/BTRCP1 and FBXW11/BTRCP2. Interactions with CUL1, BTRC and FBXW11 are enhanced upon DNA damage. Interacts with PIM1. Interacts with CHEK2; mediates CDC25A phosphorylation and degradation in response to infrared-induced DNA damages.

Protein Expression for CDC25A Gene

Selected DME Specific Peptides for CDC25A Gene

Post-translational modifications for CDC25A Gene

Phosphorylated by CHEK1 on Ser-76, Ser-124, Ser-178, Ser-279, Ser-293 and Thr-507 during checkpoint mediated cell cycle arrest. Also phosphorylated by CHEK2 on Ser-124, Ser-279, and Ser-293 during checkpoint mediated cell cycle arrest. Phosphorylation on Ser-178 and Thr-507 creates binding sites for YWHAE/14-3-3 epsilon which inhibits CDC25A. Phosphorylation on Ser-76, Ser-124, Ser-178, Ser-279 and Ser-293 may also promote ubiquitin-dependent proteolysis of CDC25A by the SCF complex. Phosphorylation of CDC25A at Ser-76 by CHEK1 primes it for subsequent phosphorylation at Ser-79, Ser-82 and Ser-88 by NEK11. Phosphorylation by NEK11 is required for BTRC-mediated polyubiquitination and degradation. Phosphorylation by PIM1 leads to an increase in phosphatase activity. Phosphorylated by PLK3 following DNA damage, leading to promote its ubiquitination and degradation.

Ubiquitinated by the anaphase promoting complex/cyclosome (APC/C) ubiquitin ligase complex that contains FZR1/CDH1 during G1 phase leading to its degradation by the proteasome. Ubiquitinated by a SCF complex containing BTRC and FBXW11 during S phase leading to its degradation by the proteasome. Deubiquitination by USP17L2/DUB3 leads to its stabilization.